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Redesigning the QA binding site of Photosystem II allows reduction of exogenous quinones

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  • Han-Yi Fu

    (Laboratoire de Physiologie Membranaire et Moléculaire du Chloroplaste, UMR 7141, Institut de Biologie Physico-Chimique, CNRS/Université Pierre et Marie Curie
    Present address: Biodiversity Research Center, Academia Sinica, Taipei 11529, Taiwan (H.-Y.F.))

  • Daniel Picot

    (Laboratoire de Biologie Physico-Chimique des Protéines Membranaires, UMR 7099, Institut de Biologie Physico-Chimique, CNRS/Université Paris Diderot, Paris 7, Paris 75005, France)

  • Yves Choquet

    (Laboratoire de Physiologie Membranaire et Moléculaire du Chloroplaste, UMR 7141, Institut de Biologie Physico-Chimique, CNRS/Université Pierre et Marie Curie)

  • Guillaume Longatte

    (Ecole Normale Supérieure-PSL Research University, Sorbonne Universités, UPMC Univ. Paris 06, CNRS UMR 8640 PASTEUR, 24, rue Lhomond, Paris 75005, France
    Present address: School of Chemistry, The University of New South Wales, Sydney, New South Wales 2052, Australia (G.L.))

  • Adnan Sayegh

    (Ecole Normale Supérieure-PSL Research University, Sorbonne Universités, UPMC Univ. Paris 06, CNRS UMR 8640 PASTEUR, 24, rue Lhomond, Paris 75005, France)

  • Jérôme Delacotte

    (Ecole Normale Supérieure-PSL Research University, Sorbonne Universités, UPMC Univ. Paris 06, CNRS UMR 8640 PASTEUR, 24, rue Lhomond, Paris 75005, France)

  • Manon Guille-Collignon

    (Ecole Normale Supérieure-PSL Research University, Sorbonne Universités, UPMC Univ. Paris 06, CNRS UMR 8640 PASTEUR, 24, rue Lhomond, Paris 75005, France)

  • Frédéric Lemaître

    (Ecole Normale Supérieure-PSL Research University, Sorbonne Universités, UPMC Univ. Paris 06, CNRS UMR 8640 PASTEUR, 24, rue Lhomond, Paris 75005, France)

  • Fabrice Rappaport

    (Laboratoire de Physiologie Membranaire et Moléculaire du Chloroplaste, UMR 7141, Institut de Biologie Physico-Chimique, CNRS/Université Pierre et Marie Curie)

  • Francis-André Wollman

    (Laboratoire de Physiologie Membranaire et Moléculaire du Chloroplaste, UMR 7141, Institut de Biologie Physico-Chimique, CNRS/Université Pierre et Marie Curie)

Abstract

Strategies to harness photosynthesis from living organisms to generate electrical power have long been considered, yet efficiency remains low. Here, we aimed to reroute photosynthetic electron flow in photosynthetic organisms without compromising their phototrophic properties. We show that 2,6-dimethyl-p-benzoquinone (DMBQ) can be used as an electron mediator to assess the efficiency of mutations designed to engineer a novel electron donation pathway downstream of the primary electron acceptor QA of Photosystem (PS) II in the green alga Chlamydomonas reinhardtii. Through the use of structural prediction studies and a screen of site-directed PSII mutants we show that modifying the environment of the QA site increases the reduction rate of DMBQ. Truncating the C-terminus of the PsbT subunit protruding in the stroma provides evidence that shortening the distance between QA and DMBQ leads to sustained electron transfer to DMBQ, as confirmed by chronoamperometry, consistent with a bypass of the natural QA°− to QB pathway.

Suggested Citation

  • Han-Yi Fu & Daniel Picot & Yves Choquet & Guillaume Longatte & Adnan Sayegh & Jérôme Delacotte & Manon Guille-Collignon & Frédéric Lemaître & Fabrice Rappaport & Francis-André Wollman, 2017. "Redesigning the QA binding site of Photosystem II allows reduction of exogenous quinones," Nature Communications, Nature, vol. 8(1), pages 1-12, August.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15274
    DOI: 10.1038/ncomms15274
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